ID G2FG19_9GAMM Unreviewed; 821 AA.
AC G2FG19;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN Name=glgP1 {ECO:0000313|EMBL:EGW54252.1};
GN ORFNames=TevJSym_ao00380 {ECO:0000313|EMBL:EGW54252.1};
OS endosymbiont of Tevnia jerichonana (vent Tica).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX NCBI_TaxID=1049564 {ECO:0000313|EMBL:EGW54252.1, ECO:0000313|Proteomes:UP000005167};
RN [1] {ECO:0000313|EMBL:EGW54252.1, ECO:0000313|Proteomes:UP000005167}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Gardebrecht A., Markert S., Felbeck H., Thuermer A., Albrecht D.,
RA Wollherr A., Kabisch J., Lehmann R., Daniel R., Liesegang H., Hecker M.,
RA Sievert S.M., Schweder T.;
RT "The endosymbionts of the deep-sea tubeworms Riftia pachyptila and Tevnia
RT jerichonana share an identical physiology as revealed by proteogenomic
RT analyses.";
RL ISME J. 0:0-0(2011).
CC -!- FUNCTION: Allosteric enzyme that catalyzes the rate-limiting step in
CC glycogen catabolism, the phosphorolytic cleavage of glycogen to produce
CC glucose-1-phosphate, and plays a central role in maintaining cellular
CC and organismal glucose homeostasis. {ECO:0000256|RuleBase:RU000587}.
CC -!- FUNCTION: Phosphorylase is an important allosteric enzyme in
CC carbohydrate metabolism. Enzymes from different sources differ in their
CC regulatory mechanisms and in their natural substrates. However, all
CC known phosphorylases share catalytic and structural properties.
CC {ECO:0000256|ARBA:ARBA00025174}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-alpha-D-glucosyl](n) + phosphate = [(1->4)-alpha-D-
CC glucosyl](n-1) + alpha-D-glucose 1-phosphate; Xref=Rhea:RHEA:41732,
CC Rhea:RHEA-COMP:9584, Rhea:RHEA-COMP:9586, ChEBI:CHEBI:15444,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58601; EC=2.4.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001275,
CC ECO:0000256|RuleBase:RU000587};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU000587};
CC -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC {ECO:0000256|ARBA:ARBA00006047, ECO:0000256|RuleBase:RU000587}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGW54252.1}.
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DR EMBL; AFZB01000015; EGW54252.1; -; Genomic_DNA.
DR RefSeq; WP_005958622.1; NZ_AFZB01000015.1.
DR AlphaFoldDB; G2FG19; -.
DR PATRIC; fig|1049564.3.peg.1856; -.
DR eggNOG; COG0058; Bacteria.
DR Proteomes; UP000005167; Unassembled WGS sequence.
DR GO; GO:0008184; F:glycogen phosphorylase activity; IEA:InterPro.
DR GO; GO:0102250; F:linear malto-oligosaccharide phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0102499; F:SHG alpha-glucan phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd04300; GT35_Glycogen_Phosphorylase; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR InterPro; IPR011833; Glycg_phsphrylas.
DR InterPro; IPR000811; Glyco_trans_35.
DR InterPro; IPR035090; Pyridoxal_P_attach_site.
DR NCBIfam; TIGR02093; P_ylase; 1.
DR PANTHER; PTHR11468; GLYCOGEN PHOSPHORYLASE; 1.
DR PANTHER; PTHR11468:SF3; GLYCOGEN PHOSPHORYLASE; 1.
DR Pfam; PF00343; Phosphorylase; 1.
DR PIRSF; PIRSF000460; Pprylas_GlgP; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR PROSITE; PS00102; PHOSPHORYLASE; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|RuleBase:RU000587};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU000587};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000460-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005167};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 669
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 821 AA; 94473 MW; DED22EB525D5EEF7 CRC64;
MSSSNRFKFD FLASKPKAIQ RSVSNHLVYT IGKDPFTATD HDWMMAFCHV VRDRLIERWM
ETQRSYYRND AKRVYYLSME FLIGRSLTNS LLNMDIHDAC SSALHRLGIE LERLRNLEHD
AALGNGGLGR LAACFLDSMA TLDLPGIGYG IRFEYGMFRQ RIENGQQVEH PENWLAHGNP
WEFPRPEVAY KVRFGGRVLE YQGPNGRRQF DWIEGDLVLA QAYDTPIPGY KNDTVNNLRL
WSAKAHQAFD LSCFNMGEYS SAVEEKTLSE NISKVLYPDD SSSQNRELRL KQQYFFVCAS
LKDILRRFFS DHNDIHELPE RVAIQLNDTH PAIAIPELMR VLIDKYHLEW QLAWEITTKI
FSYTNHTLLP EALESWPVEL LGRLLPRHLQ LIYEINRRFL LMVANLHPGD TERQRRLSVI
DEQDGRRVRM AHLAIIGSHK VNGVSALHSG LLKSSTFHDF DEFYPNKIIN ITNGITPRRW
LYQANRPLSA LICEAIGDAW VRDLNQLEAL IPLADDSSFQ ERFAAAKLVN KQRLAELVKF
HLGQQIDPHT LFDVQVKRIH EYKRQLLNLM RVIAHYNRLL DAPDAEVVPR TYIFGGKAAP
GYFMAKLIIR LINDVADVID NDQAVNKRLK VLFIPNYDVT TAADIIPAAE LSQQISTAGM
EASGTGNMKL ALNGSLTMGT LDGANVEIRD QVGAENIFIF GLTTDQVKQR CQQGYHPRYH
FESEPLLRRV VEMIGNGFFS PEEPERYKPL VESLLDRDHF MVMADFQAYL ECSDRADAIY
RQPEIWNQMA ILNTAQMGYF SSDRTIQEYA QQIWQIAPIQ R
//
